(data stored in ACNUC7421 zone)

SWISSPROT: Q8X966_ECO57

ID   Q8X966_ECO57            Unreviewed;       630 AA.
AC   Q8X966; Q7AHP9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   30-AUG-2017, entry version 129.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=aceF {ECO:0000313|EMBL:AAG54419.1};
GN   OrderedLocusNames=ECs0119 {ECO:0000313|EMBL:BAB33542.1}, Z0125
GN   {ECO:0000313|EMBL:AAG54419.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB33542.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33542.1};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2] {ECO:0000313|EMBL:AAG54419.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54419.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G.III., Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [3] {ECO:0000213|PDB:4N72}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 382-630.
RX   PubMed=24742683; DOI=10.1074/jbc.M113.544080;
RA   Wang J., Nemeria N.S., Chandrasekhar K., Kumaran S., Arjunan P.,
RA   Reynolds S., Calero G., Brukh R., Kakalis L., Furey W., Jordan F.;
RT   "Structure and function of the catalytic domain of the dihydrolipoyl
RT   acetyltransferase component in Escherichia coli pyruvate dehydrogenase
RT   complex.";
RL   J. Biol. Chem. 289:15215-15230(2014).
RN   [4] {ECO:0000213|PDB:4QOY}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 327-372.
RX   PubMed=25210042; DOI=10.1074/jbc.M114.592915;
RA   Arjunan P., Wang J., Nemeria N.S., Reynolds S., Brown I.,
RA   Chandrasekhar K., Calero G., Jordan F., Furey W.;
RT   "Novel binding motif and new flexibility revealed by structural
RT   analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase
RT   subcomplex from the Escherichia coli pyruvate dehydrogenase
RT   multienzyme complex.";
RL   J. Biol. Chem. 289:30161-30176(2014).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 3 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE005174; AAG54419.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33542.1; -; Genomic_DNA.
DR   PIR; G85494; G85494.
DR   PIR; G90643; G90643.
DR   RefSeq; NP_308146.1; NC_002695.1.
DR   RefSeq; WP_000963555.1; NZ_LPWC02000002.1.
DR   PDB; 4N72; X-ray; 2.25 A; A/B/C=382-630.
DR   PDB; 4QOY; X-ray; 2.80 A; E/F=327-372.
DR   PDBsum; 4N72; -.
DR   PDBsum; 4QOY; -.
DR   SMR; Q8X966; -.
DR   STRING; 155864.Z0125; -.
DR   EnsemblBacteria; AAG54419; AAG54419; Z0125.
DR   EnsemblBacteria; BAB33542; BAB33542; BAB33542.
DR   GeneID; 913659; -.
DR   KEGG; ece:Z0125; -.
DR   KEGG; ecs:ECs0119; -.
DR   PATRIC; fig|386585.9.peg.217; -.
DR   eggNOG; ENOG4107QSN; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281562; -.
DR   KO; K00627; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178:SF4; PTHR43178:SF4; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 3.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 3.
DR   TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR   PROSITE; PS00189; LIPOYL; 3.
PE   1: Evidence at protein level;
DR   PRODOM; Q8X966.
DR   SWISS-2DPAGE; Q8X966.
KW   3D-structure {ECO:0000213|PDB:4N72, ECO:0000213|PDB:4QOY};
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AAG54419.1};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN        2     75       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      105    178       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      206    279       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   630 AA;  66184 MW;  454F561F818285FC CRC64;
     MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS
     VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAVP EAAAAKDVNV PDIGSDEVEV
     TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNTGDKVST GSLIMVFEVA
     GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT
     VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
     AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED
     VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW
     VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS
     LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA
     GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
     FDHRVIDGAD GARFITIINN TLSDIRRLVM
//

If you have problems or comments...

PBIL Back to PBIL home page